Functional analysis of a conserved region of the baculovirus envelope fusion protein, LD130.

The envelope fusion protein from a baculovirus pathogenic for Lymantria dispar was characterized. N-terminal sequence analysis determined that it was cleaved downstream of predicted signal peptide and furin cleavage motifs. Mutation of the furin motif resulted in a protein that was not cleaved and did not mediate fusion.

Transcriptional mapping of two genes encoding baculovirus envelope-associated proteins.

Genes encoding two representatives of the LD130 family of baculovirus envelope-associated proteins were transcriptionally mapped. These included ld130, which encodes a low pH-induced envelope fusion protein of the Lymantria dispar multinucleocapsid nucleopolyhedrovirus, and op21, which is related to ld130 but is encoded by Orgyia pseudotsugata MNPV and appears to lack an envelope fusion activity. The size and temporal expression of mRNA of both genes were examined by Northern blot analysis of RNA extracted from infected cells at selected timepoints.